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P32 of caspase-11 mutant C254A

Analyse P32 of caspase-11 mutant C254A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6KMT
Type
protein
Length
935 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Caspase-4
EC
3.4.22.64
UniProt
P70343
Pockets
4 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CCaspase-4 (EC 3.4.22.64)protein23435% helix, 22% strandP70343
DCaspase-4 (EC 3.4.22.64)protein23334% helix, 22% strandP70343

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16040.780.8456empty
26380.760.8248empty
34340.600.7640empty
4730.310.7423empty

Interfaces

3 interfaces between chains.

  • A–B · 1179 Ų buried · 22 hydrogen bonds · protein-protein
  • C–D · 1148 Ų buried · 19 hydrogen bonds · protein-protein
  • A–C · 683 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 6KMT · P32 of caspase-11 mutant C254A · the same entry in another collection · chain D against D, TM-score 1.00
  • P70343 · AlphaFold monomer V2.0 prediction for caspase-4 (P70343) · a predicted model of the same protein · chain B against A, TM-score 0.97

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